Evidence map›Paper›PMID 32781559›Full record

ReviewMolecules (Basel, Switzerland)2020

Catechins as Tools to Understand the Molecular Basis of Neurodegeneration.

Karla Martinez Pomier, Rashik Ahmed, Giuseppe Melacini

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  9. Natural Compounds as Inhibitors of Aβ Peptide and Tau Aggregation.CNS & neurological disorders drug targets · 2024
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  12. Identification of Catechins' Binding Sites in Monomeric AInternational journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Karla Martinez PomierDepartment of Chemistry and Chemical Biology, McMaster University, Hamilton, ON L8S 4M1, Canada.
Rashik AhmedDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON L8S 4M1, Canada.
Giuseppe MelaciniDepartment of Chemistry and Chemical Biology, McMaster University, Hamilton, ON L8S 4M1, Canada.ORCID 0000-0003-1164-2853

Funding

Natural Sciences and Engineering Research Council of Canada RGPIN-2019-05990
6 · The paper itself

Abstract

Protein misfolding as well as the subsequent self-association and deposition of amyloid aggregates is implicated in the progression of several neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Modulators of amyloidogenic aggregation serve as essential tools to dissect the underlying molecular mechanisms and may offer insight on potential therapeutic solutions. These modulators include green tea catechins, which are potent inhibitors of amyloid aggregation. Although catechins often exhibit poor pharmacokinetic properties and bioavailability, they are still essential tools for identifying the drivers of amyloid aggregation and for developing other aggregation modulators through structural mimicry. As an illustration of such strategies, here we review how catechins have been used to map the toxic surfaces of oligomeric amyloid-like species and develop catechin-based phenolic compounds with enhanced anti-amyloid activity.

Indexed as

Neurodegenerative DiseasesCatechinHumansMolecular Targeted TherapyNeuroprotective AgentsCatechinNeuroprotective AgentsAlzheimer’s Diseaseamyloid betacatechinEGCGNMRα-synuclein

Identifiers

PMID32781559
PMCPMC7465241

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.